Effect of troponin-tropomyosin complex and Ca2+ on conformational changes in F-actin induced by myosin subfragment-1

Авторы: Borovikov Y.S., Gusev N.B.
Журнал: European Journal of Biochemistry
Том: 136
Номер: 2
Год издания: 1983
Первая страница: 363
Последняя страница: 369
DOI: 10.1111/j.1432-1033.1983.tb07750.x
Аннотация: The interaction of regulated and unregulated actin of myosin-free ghost single fibre with myosin subfragment-1 free of 5,5’-dithiobis(2-nitrobenzoic acid) light chains was investigated by polarized microphotometry. The anisotropy of intrinsic tryptophan fluorescence of regulated actin is Ca2+-dependent and has a maximal value at low (pCa greater than or equal to 7) and a minimal value at high (pCa less than or equal to 6) concentrations of Ca2+. The interaction of myosin subfragment-1 with actin induces cooperative changes in actin structure, which manifest themselves in a decrease in the anisotropy of tryptophan fluorescence. The cooperativity of conformational changes in actin, induced by myosin subfragment-1, is high for regulated actin in the absence of Ca2+ and low for unregulated and regulated actin in the presence of Ca2+. The data obtained suggest that the decrease of the flexibility of actin filaments, induced by tropomyosin or by Ca-unsaturated troponin-tropomyosin complex, results in increased cooperativity of conformational changes of actin induced by myosin subfragment-1.
Добавил в систему: Гусев Николай Борисович

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